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Results 1 - 10 of 10
EC Number
General Information
Commentary
Reference
malfunction
cathepsin X prevents an effective immune response against Helicobacter pylori infection of THP-1 cells, overview
physiological function
active cathepsin X enhances adhesion of monocytes/macrophages to fibrinogen and regulates the phagocytosis. By activation of Mac-1 receptor cathepsin X may regulate also the maturation of dendritic cells, a process, which is crucial in the initiation of adaptive immunity. Cathepsin X activates also the other ?2 integrin receptor, LFA-1, which is involved in the proliferation of T lymphocytes. By modulating the activity of LFA-1 cathepsin X causes cytoskeletal rearrangements and morphological changes of T lymphocytes enhancing ameboid-like migration in 2-D and 3-D barriers and increasing homotypic aggregation. The cleavage of C-terminal amino acids of alpha and gamma enolase by cathepsin X abolishes their neurotrophic activity affecting neuronal cell survival and neuritogenesis. Role of cathepsin X in cell signaling, detailed overview
physiological function
cathepsin B2 is expressed only in early stages of the parasite and may be involved in digestion of host connective tissues and evasion of the host immune system during their penetration and migration
physiological function
cathepsin X generates peptide receptor agonists and acts as a type I kininase. It is a cysteine-type carboxypeptidase and able to modulate the kallikrein–kinin system through carboxyterminal processing of the small peptide hormones bradykinin and kallidin. Cathepsin X as an alternative possible link between the kallikrein–kinin system and the renin–angiotensin system in that it not only cleaves kinins C-terminally, but also converts angiotensin I to angiotensin II, reaction of EC 3.6.15.1
physiological function
cathepsin X, a cysteine protease, regulates T-cell migration by interaction with lymphocyte function associated antigen-1, LFA-1. Gradual cleavage of LFA-1 by cathepsin X enables the transition between intermediate and high affinity LFA-1, an event that is crucial for effective T-cell migration, overview
physiological function
cathepsin X-mediated beta2 integrin activation results in membrane nanotube outgrowth, nanotube structures and mechanism of membrane nanotube formation in T cells through LFA-1 integrin activation by the cysteine protease cathepsin X, mechanism of nanotube formation follows homotypic T cell contact formation,mechanism pf LFA-1 iuntegrin activation, overview
physiological function
cysteine cathepsin proteases are primarily involved in endolysosomal degradation, but also function extracellularly and in the nucleus. Cathepsin X is secreted by human osteoblasts, digests CXCL-12 and impairs adhesion of hematopoietic stem and progenitor cells, i.e. HSPC s, to osteoblasts. Cathepsin X can influence HSPC trafficking in the bone marrow
physiological function
downregulation of cathepsin X expression by siRNA attenuates the neuronal death caused by 6-hydroxydopamine. Treatment with specific cathepsin X inhibitor AMS36 protects cells against 6-hydroxydopamine mediated cytotoxicity, resulting in reduced cell death and apoptosis.Inhibitor AMS36 reverses 6-hydroxydopamine-induced loss of tyrosine hydroxylase and attenuates 6-hydroxydopamine-induced activation of caspase-3. Cathepsin X may be responsible for dopamine neuron death, involved in the pathogenic cascade event for the neurodegenerative disorders, such as Parkinson's disease
physiological function
RNAi for cathepsins L and Z confirms that they are critical in degrading polyglutamine-rich proteins (expanded huntingtin exon 1) but not other types of aggregation-prone proteins
physiological function
synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice, overview
Results 1 - 10 of 10